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P0A7P5

- RL34_ECOLI

UniProt

P0A7P5 - RL34_ECOLI

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Protein

50S ribosomal protein L34

Gene

rpmH

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli

Display
All None

  • Function
  • Names & Taxonomy
  • Subcellular locationSubcell. location
  • Pathology & BiotechPathol./Biotech
  • PTM / Processing
  • Expression
  • Interaction
  • Structure
  • Family & Domains
  • Sequence
  • Cross-references
  • Publications
  • Entry information
  • Miscellaneous
  • Similar proteins
Top

Functioni

GO - Molecular functioni

  1. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. translation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciEcoCyc:EG10892-MONOMER.
ECOL316407:JW3680-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L34
Gene namesi
Name:rpmH
Synonyms:rimA, ssaF
Ordered Locus Names:b3703, JW3680
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10892. rpmH.

Subcellular locationi

GO - Cellular componenti

  1. ribosome Source: UniProtKB-KW
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 464650S ribosomal protein L34PRO_0000187377Add
BLAST

Proteomic databases

PaxDbiP0A7P5.
PRIDEiP0A7P5.

Expressioni

Gene expression databases

GenevestigatoriP0A7P5.

Interactioni

Protein-protein interaction databases

DIPiDIP-581N.
IntActiP0A7P5. 3 interactions.
STRINGi511145.b3703.

Structurei

Secondary structure

1
46
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 168Combined sources
Helixi18 – 225Combined sources
Helixi25 – 3612Combined sources
Beta strandi42 – 443Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VS6X-ray3.4621-46[»]
1VS8X-ray3.4621-46[»]
1VT2X-ray3.3021-46[»]
2AW4X-ray3.4621-46[»]
2AWBX-ray3.4621-46[»]
2I2TX-ray3.2221-46[»]
2I2VX-ray3.2221-46[»]
2J28electron microscopy8.0021-46[»]
2QAMX-ray3.2121-46[»]
2QAOX-ray3.2121-46[»]
2QBAX-ray3.5421-46[»]
2QBCX-ray3.5421-46[»]
2QBEX-ray3.3021-46[»]
2QBGX-ray3.3021-46[»]
2QBIX-ray4.0021-46[»]
2QBKX-ray4.0021-46[»]
2QOVX-ray3.9321-46[»]
2QOXX-ray3.9321-46[»]
2QOZX-ray3.5021-46[»]
2QP1X-ray3.5021-46[»]
2RDOelectron microscopy9.1021-46[»]
2VHMX-ray3.7421-46[»]
2VHNX-ray3.7421-46[»]
2WWQelectron microscopy5.8061-46[»]
2Z4LX-ray4.4521-46[»]
2Z4NX-ray4.4521-46[»]
3BBXelectron microscopy10.0021-46[»]
3DF2X-ray3.5021-46[»]
3DF4X-ray3.5021-46[»]
3E1Belectron microscopy-V1-46[»]
3E1Delectron microscopy-V1-46[»]
3FIKelectron microscopy6.7021-46[»]
3I1NX-ray3.1921-46[»]
3I1PX-ray3.1921-46[»]
3I1RX-ray3.8121-46[»]
3I1TX-ray3.8121-46[»]
3I20X-ray3.7121-46[»]
3I22X-ray3.7121-46[»]
3IZTelectron microscopy-e1-46[»]
3IZUelectron microscopy-e1-46[»]
3J01electron microscopy-21-46[»]
3J0Telectron microscopy12.1051-46[»]
3J0Welectron microscopy14.7051-46[»]
3J0Yelectron microscopy13.5051-46[»]
3J11electron microscopy13.1051-46[»]
3J12electron microscopy11.5051-46[»]
3J14electron microscopy11.5051-46[»]
3J19electron microscopy8.3021-46[»]
3J37electron microscopy9.8071-46[»]
3J4Xelectron microscopy12.0021-46[»]
3J50electron microscopy20.0021-46[»]
3J51electron microscopy17.0021-46[»]
3J52electron microscopy12.0021-46[»]
3J54electron microscopy13.0021-46[»]
3J56electron microscopy15.0021-46[»]
3J58electron microscopy17.0021-46[»]
3J5Aelectron microscopy12.0021-46[»]
3J5Celectron microscopy17.0021-46[»]
3J5Eelectron microscopy17.0021-46[»]
3J5Gelectron microscopy20.0021-46[»]
3J5Ielectron microscopy15.0021-46[»]
3J5Kelectron microscopy9.0021-46[»]
3J5Lelectron microscopy6.6021-46[»]
3J5Oelectron microscopy6.8021-46[»]
3J5Uelectron microscopy7.6051-46[»]
3J5Welectron microscopy7.6061-46[»]
3J7Zelectron microscopy3.9021-46[»]
3KCRelectron microscopy-21-46[»]
3OASX-ray3.2521-46[»]
3OATX-ray3.2521-46[»]
3OFCX-ray3.1921-46[»]
3OFDX-ray3.1921-46[»]
3OFQX-ray3.1021-46[»]
3OFRX-ray3.1021-46[»]
3OFZX-ray3.2921-46[»]
3OG0X-ray3.2921-46[»]
3ORBX-ray3.3021-46[»]
3R8SX-ray3.0021-46[»]
3R8TX-ray3.0021-46[»]
3SGFX-ray3.2061-46[»]
3UOSX-ray3.7061-46[»]
4CSUelectron microscopy5.5061-46[»]
4GARX-ray3.3021-46[»]
4GAUX-ray3.3021-46[»]
4KIXX-ray2.9021-46[»]
4KIZX-ray2.9021-46[»]
4KJ1X-ray2.9021-46[»]
4KJ3X-ray2.9021-46[»]
4KJ5X-ray2.9021-46[»]
4KJ7X-ray2.9021-46[»]
4KJ9X-ray2.9021-46[»]
4KJBX-ray2.9021-46[»]
4PEBX-ray2.9521-46[»]
4PECX-ray2.9521-46[»]
4TOMX-ray3.0021-46[»]
4TOOX-ray3.0021-46[»]
4TOVX-ray2.9021-46[»]
4TOXX-ray2.9021-46[»]
4TP1X-ray2.9021-46[»]
4TP3X-ray2.9021-46[»]
4TP5X-ray2.9021-46[»]
4TP7X-ray2.9021-46[»]
4TP9X-ray2.8021-46[»]
4TPBX-ray2.8021-46[»]
4TPDX-ray2.8021-46[»]
4TPFX-ray2.8021-46[»]
4UY8electron microscopy3.8021-46[»]
4WAPX-ray3.0921-46[»]
4WARX-ray3.0921-46[»]
ProteinModelPortaliP0A7P5.
SMRiP0A7P5. Positions 1-46.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7P5.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L34P family.Curated

Phylogenomic databases

eggNOGiCOG0230.
HOGENOMiHOG000111572.
InParanoidiP0A7P5.
KOiK02914.
OrthoDBiEOG6DZF71.
PhylomeDBiP0A7P5.

Family and domain databases

HAMAPiMF_00391. Ribosomal_L34.
InterProiIPR000271. Ribosomal_L34.
IPR020939. Ribosomal_L34_CS.
[Graphical view]
PANTHERiPTHR14503. PTHR14503. 1 hit.
PfamiPF00468. Ribosomal_L34. 1 hit.
[Graphical view]
ProDomiPD003101. Ribosomal_L34. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsiTIGR01030. rpmH_bact. 1 hit.
PROSITEiPS00784. RIBOSOMAL_L34. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A7P5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40 
MKRTFQPSVL KRNRSHGFRA RMATKNGRQV LARRRAKGRA RLTVSK
Length:46
Mass (Da):5,380
Last modified:July 21, 1986 - v1
Checksum:i600916E398939412
GO

Mass spectrometryi

Molecular mass is 5380.5 Da from positions 1 - 46. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01602 Genomic DNA. Translation: AAB59148.1.
X01861 Genomic DNA. Translation: CAA25982.1.
M11056 Genomic DNA. Translation: AAA24566.1.
L10328 Genomic DNA. Translation: AAA62054.1.
U00096 Genomic DNA. Translation: AAC76726.1.
AP009048 Genomic DNA. Translation: BAE77591.1.
RefSeqiNP_418158.1. NC_000913.3.
YP_491732.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76726; AAC76726; b3703.
BAE77591; BAE77591; BAE77591.
GeneIDi12930542.
948216.
KEGGiecj:Y75_p3470.
eco:b3703.
PATRICi32122903. VBIEscCol129921_3827.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
 J01602 Genomic DNA. Translation: AAB59148.1 .
X01861 Genomic DNA. Translation: CAA25982.1 .
M11056 Genomic DNA. Translation: AAA24566.1 .
L10328 Genomic DNA. Translation: AAA62054.1 .
U00096 Genomic DNA. Translation: AAC76726.1 .
AP009048 Genomic DNA. Translation: BAE77591.1 .
RefSeqi NP_418158.1. NC_000913.3.
YP_491732.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1VS6 X-ray 3.46 2 1-46 [» ]
1VS8 X-ray 3.46 2 1-46 [» ]
1VT2 X-ray 3.30 2 1-46 [» ]
2AW4 X-ray 3.46 2 1-46 [» ]
2AWB X-ray 3.46 2 1-46 [» ]
2I2T X-ray 3.22 2 1-46 [» ]
2I2V X-ray 3.22 2 1-46 [» ]
2J28 electron microscopy 8.00 2 1-46 [» ]
2QAM X-ray 3.21 2 1-46 [» ]
2QAO X-ray 3.21 2 1-46 [» ]
2QBA X-ray 3.54 2 1-46 [» ]
2QBC X-ray 3.54 2 1-46 [» ]
2QBE X-ray 3.30 2 1-46 [» ]
2QBG X-ray 3.30 2 1-46 [» ]
2QBI X-ray 4.00 2 1-46 [» ]
2QBK X-ray 4.00 2 1-46 [» ]
2QOV X-ray 3.93 2 1-46 [» ]
2QOX X-ray 3.93 2 1-46 [» ]
2QOZ X-ray 3.50 2 1-46 [» ]
2QP1 X-ray 3.50 2 1-46 [» ]
2RDO electron microscopy 9.10 2 1-46 [» ]
2VHM X-ray 3.74 2 1-46 [» ]
2VHN X-ray 3.74 2 1-46 [» ]
2WWQ electron microscopy 5.80 6 1-46 [» ]
2Z4L X-ray 4.45 2 1-46 [» ]
2Z4N X-ray 4.45 2 1-46 [» ]
3BBX electron microscopy 10.00 2 1-46 [» ]
3DF2 X-ray 3.50 2 1-46 [» ]
3DF4 X-ray 3.50 2 1-46 [» ]
3E1B electron microscopy - V 1-46 [» ]
3E1D electron microscopy - V 1-46 [» ]
3FIK electron microscopy 6.70 2 1-46 [» ]
3I1N X-ray 3.19 2 1-46 [» ]
3I1P X-ray 3.19 2 1-46 [» ]
3I1R X-ray 3.81 2 1-46 [» ]
3I1T X-ray 3.81 2 1-46 [» ]
3I20 X-ray 3.71 2 1-46 [» ]
3I22 X-ray 3.71 2 1-46 [» ]
3IZT electron microscopy - e 1-46 [» ]
3IZU electron microscopy - e 1-46 [» ]
3J01 electron microscopy - 2 1-46 [» ]
3J0T electron microscopy 12.10 5 1-46 [» ]
3J0W electron microscopy 14.70 5 1-46 [» ]
3J0Y electron microscopy 13.50 5 1-46 [» ]
3J11 electron microscopy 13.10 5 1-46 [» ]
3J12 electron microscopy 11.50 5 1-46 [» ]
3J14 electron microscopy 11.50 5 1-46 [» ]
3J19 electron microscopy 8.30 2 1-46 [» ]
3J37 electron microscopy 9.80 7 1-46 [» ]
3J4X electron microscopy 12.00 2 1-46 [» ]
3J50 electron microscopy 20.00 2 1-46 [» ]
3J51 electron microscopy 17.00 2 1-46 [» ]
3J52 electron microscopy 12.00 2 1-46 [» ]
3J54 electron microscopy 13.00 2 1-46 [» ]
3J56 electron microscopy 15.00 2 1-46 [» ]
3J58 electron microscopy 17.00 2 1-46 [» ]
3J5A electron microscopy 12.00 2 1-46 [» ]
3J5C electron microscopy 17.00 2 1-46 [» ]
3J5E electron microscopy 17.00 2 1-46 [» ]
3J5G electron microscopy 20.00 2 1-46 [» ]
3J5I electron microscopy 15.00 2 1-46 [» ]
3J5K electron microscopy 9.00 2 1-46 [» ]
3J5L electron microscopy 6.60 2 1-46 [» ]
3J5O electron microscopy 6.80 2 1-46 [» ]
3J5U electron microscopy 7.60 5 1-46 [» ]
3J5W electron microscopy 7.60 6 1-46 [» ]
3J7Z electron microscopy 3.90 2 1-46 [» ]
3KCR electron microscopy - 2 1-46 [» ]
3OAS X-ray 3.25 2 1-46 [» ]
3OAT X-ray 3.25 2 1-46 [» ]
3OFC X-ray 3.19 2 1-46 [» ]
3OFD X-ray 3.19 2 1-46 [» ]
3OFQ X-ray 3.10 2 1-46 [» ]
3OFR X-ray 3.10 2 1-46 [» ]
3OFZ X-ray 3.29 2 1-46 [» ]
3OG0 X-ray 3.29 2 1-46 [» ]
3ORB X-ray 3.30 2 1-46 [» ]
3R8S X-ray 3.00 2 1-46 [» ]
3R8T X-ray 3.00 2 1-46 [» ]
3SGF X-ray 3.20 6 1-46 [» ]
3UOS X-ray 3.70 6 1-46 [» ]
4CSU electron microscopy 5.50 6 1-46 [» ]
4GAR X-ray 3.30 2 1-46 [» ]
4GAU X-ray 3.30 2 1-46 [» ]
4KIX X-ray 2.90 2 1-46 [» ]
4KIZ X-ray 2.90 2 1-46 [» ]
4KJ1 X-ray 2.90 2 1-46 [» ]
4KJ3 X-ray 2.90 2 1-46 [» ]
4KJ5 X-ray 2.90 2 1-46 [» ]
4KJ7 X-ray 2.90 2 1-46 [» ]
4KJ9 X-ray 2.90 2 1-46 [» ]
4KJB X-ray 2.90 2 1-46 [» ]
4PEB X-ray 2.95 2 1-46 [» ]
4PEC X-ray 2.95 2 1-46 [» ]
4TOM X-ray 3.00 2 1-46 [» ]
4TOO X-ray 3.00 2 1-46 [» ]
4TOV X-ray 2.90 2 1-46 [» ]
4TOX X-ray 2.90 2 1-46 [» ]
4TP1 X-ray 2.90 2 1-46 [» ]
4TP3 X-ray 2.90 2 1-46 [» ]
4TP5 X-ray 2.90 2 1-46 [» ]
4TP7 X-ray 2.90 2 1-46 [» ]
4TP9 X-ray 2.80 2 1-46 [» ]
4TPB X-ray 2.80 2 1-46 [» ]
4TPD X-ray 2.80 2 1-46 [» ]
4TPF X-ray 2.80 2 1-46 [» ]
4UY8 electron microscopy 3.80 2 1-46 [» ]
4WAP X-ray 3.09 2 1-46 [» ]
4WAR X-ray 3.09 2 1-46 [» ]
ProteinModelPortali P0A7P5.
SMRi P0A7P5. Positions 1-46.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-581N.
IntActi P0A7P5. 3 interactions.
STRINGi 511145.b3703.

Chemistry

ChEMBLi CHEMBL2363135.

Proteomic databases

PaxDbi P0A7P5.
PRIDEi P0A7P5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76726 ; AAC76726 ; b3703 .
BAE77591 ; BAE77591 ; BAE77591 .
GeneIDi 12930542.
948216.
KEGGi ecj:Y75_p3470.
eco:b3703.
PATRICi 32122903. VBIEscCol129921_3827.

Organism-specific databases

EchoBASEi EB0885.
EcoGenei EG10892. rpmH.

Phylogenomic databases

eggNOGi COG0230.
HOGENOMi HOG000111572.
InParanoidi P0A7P5.
KOi K02914.
OrthoDBi EOG6DZF71.
PhylomeDBi P0A7P5.

Enzyme and pathway databases

BioCyci EcoCyc:EG10892-MONOMER.
ECOL316407:JW3680-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A7P5.
PROi P0A7P5.

Gene expression databases

Genevestigatori P0A7P5.

Family and domain databases

HAMAPi MF_00391. Ribosomal_L34.
InterProi IPR000271. Ribosomal_L34.
IPR020939. Ribosomal_L34_CS.
[Graphical view ]
PANTHERi PTHR14503. PTHR14503. 1 hit.
Pfami PF00468. Ribosomal_L34. 1 hit.
[Graphical view ]
ProDomi PD003101. Ribosomal_L34. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
TIGRFAMsi TIGR01030. rpmH_bact. 1 hit.
PROSITEi PS00784. RIBOSOMAL_L34. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The sequence determination of a protein in a micro scale: the sequence analysis of ribosomal protein L34 of Escherichia coli."
    Chen R.
    Hoppe-Seyler's Z. Physiol. Chem. 357:873-886(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Strain: K12.
  2. "The nucleotide sequence of the dnaA gene promoter and of the adjacent rpmH gene, coding for the ribosomal protein L34, of Escherichia coli."
    Hansen F.G., Hansen E.B., Atlung T.
    EMBO J. 1:1043-1048(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Physical mapping and nucleotide sequence of the rnpA gene that encodes the protein component of ribonuclease P in Escherichia coli."
    Hansen F.G., Hansen E.B., Atlung T.
    Gene 38:85-93(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  4. "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication."
    Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.
    Genomics 16:551-561(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  6. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  7. "Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry."
    Arnold R.J., Reilly J.P.
    Anal. Biochem. 269:105-112(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
    Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
  8. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.
+Additional computationally mapped references.

Entry informationi

Entry nameiRL34_ECOLI
AccessioniPrimary (citable) accession number: P0A7P5
Secondary accession number(s): P02437, Q2M815
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 7, 2015
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Ribosomal proteins
    Ribosomal proteins families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.
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